Journal
LANGMUIR
Volume 27, Issue 1, Pages 19-24Publisher
AMER CHEMICAL SOC
DOI: 10.1021/la104264f
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Funding
- Romanian Ministry of Research and Technology [PN-2 62-061]
- Alexandru I. Cuza University
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The study of factors essential for protein-peptide interactions and protein pore-mediated peptide transport are of particular relevance in biology. Wild-type alpha-hemolysin was adopted as a nanoreactor in which perturbations of the current through a protein containing a lumen-residing, aryl-capped antimicrobial peptide were seen for the first time and studied at the single-molecule level. Energy and steric considerations hint that Met-aryl interactions between aromatic residues placed at a peptide's extremities and any of the methionines lining the alpha-hemolysin constriction region may be the primary cause of peptide stabilization within the lumen and may be particularly important to the peptide-alpha-hemolysin interaction.
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